Research workbench
Structural insights into novel mechanisms of inhibition of the major b-carbonic anhydrase CafB from the pathogenic fungus Aspergillus fumigatus (disulfide-bonded form)
Analyse Structural insights into novel mechanisms of inhibition of the major b-carbonic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CXX
- Type
- protein
- Length
- 417 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
- Molecule
- Carbonic anhydrase
- EC
- 4.2.1.1
- UniProt
- A4DA32
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.75
Structure
x-ray diffraction · resolution 2 · 2 distinct chains · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase (EC 4.2.1.1) | protein | 216 | 54% helix, 13% strand | A4DA32 |
| B | Carbonic anhydrase (EC 4.2.1.1) | protein | 201 | 51% helix, 14% strand | A4DA32 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.75 | 0.97 | 22 | SO4 |
| 2 | 203 | 0.61 | 0.82 | 32 | empty |
| 3 | 133 | 0.45 | 0.77 | 29 | empty |
| 4 | 66 | 0.39 | 0.80 | 13 | empty |
| 5 | 87 | 0.38 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 3057 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7CXX · Structural insights into novel mechanisms of inhibition of the major B-carbonic anhydrase… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A4DA32
- Elsewhere: RCSB PDB 7CXX · PDBe 7CXX · UniProt A4DA32
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